ArticleThe journal of physical chemistry. B2017
Transmembrane Pore Structures of β-Hairpin Antimicrobial Peptides by All-Atom Simulations.
Article in The journal of physical chemistry. B, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 27 citations in OpenAlex.
- Comparative in vitro screening identifies beta-hairpin antimicrobial peptide leads against Piscirickettsia salmonis, supported by membrane-level molecular dynamics.BMC microbiology · 2026Article
- Pore Formation by Amyloid-like Peptides: Effects of the Nonpolar-Polar Sequence Pattern.ACS chemical neuroscience · 2024Article
- Insights into the Adsorption Mechanisms of the Antimicrobial Peptide CIDEM-501 on Membrane Models.Antibiotics (Basel, Switzerland) · 2024Article
- Outer membrane protein evolution.Current opinion in structural biology · 2021Review
- Tuning of a Membrane-Perforating Antimicrobial Peptide to Selectively Target Membranes of Different Lipid Composition.The Journal of membrane biology · 2021Article
- Article
- Review
- Experimental and Computational Characterization of Oxidized and Reduced Protegrin Pores in Lipid Bilayers.The Journal of membrane biology · 2020Article
- What Makes a Good Pore Former: A Study of Synthetic Melittin Derivatives.Biophysical journal · 2020Article
- Lipid Head Group Parameterization for GROMOS 54A8: A Consistent Approach with Protein Force Field Description.Journal of chemical theory and computation · 2019Article
- Insights into Membrane Translocation of Protegrin Antimicrobial Peptides by Multistep Molecular Dynamics Simulations.ACS omega · 2018Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Protegrin-1 is an 18-residue β-hairpin antimicrobial peptide (AMP) that has been suggested to form transmembrane β-barrels in biological membranes. However, alternative structures have also been proposed. Here, we performed multimicrosecond, all-atom molecular dynamics simulations of various protegrin-1 oligomers on the membrane surface and in transmembrane topologies. The membrane surface simulations indicated that protegrin dimers are stable, whereas trimers and tetramers break down. Tetrameric arcs remained stably inserted in lipid membranes, but the pore water was displaced by lipid molecules. Unsheared protegrin β-barrels opened into β-sheets that surrounded stable aqueous pores, whereas tilted barrels with sheared hydrogen bonding patterns were stable in most topologies. A third type of observed pore consisted of multiple small oligomers surrounding a small, partially lipidic pore. We also considered the β-hairpin AMP tachyplesin, which showed less tendency to oligomerize than protegrin: the octameric bundle resulted in small pores surrounded by six peptides as monomers and dimers, with some peptides returning to the membrane surface. The results imply that multiple configurations of protegrin oligomers may produce aqueous pores and illustrate the relationship between topology and putative steps in protegrin-1's pore formation. However, the long-term stability of these structures needs to be assessed further.
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Registered trials
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